1QIN

HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1qina_	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase I (lactoylglutathione lyase)	Glyoxalase I (lactoylglutathione lyase)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1qinb_	Alpha and beta proteins (a+b)	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Glyoxalase I (lactoylglutathione lyase)	Glyoxalase I (lactoylglutathione lyase)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8034905	3000739	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	8034905	3000739	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyoxalase_1	e1qinA2	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_1	ECOD (1.6)
A	Glyoxalase_6	e1qinA1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_6	ECOD (1.6)
B	Glyoxalase_1	e1qinB2	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_1	ECOD (1.6)
B	Glyoxalase_6	e1qinB1	A: a+b two layers	X: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	H: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase (From Topology)	T: Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	F: Glyoxalase_6	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)
B	3.10.180.10	Alpha Beta	Roll	2,3-Dihydroxybiphenyl 1,2-Dioxygenase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00903	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily (Glyoxalase)	Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (LACTOYLGLUTATHIONE LYASE)	carbon-sulfur lyase activity lactoylglutathione lyase activity lyase activity catalytic activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	ketone metabolic process metabolic process cellular process aldehyde metabolic process methylglyoxal metabolic process carbohydrate metabolic process primary metabolic process regulation of biological process regulation of cellular process negative regulation of programmed cell death regulation of apoptotic process biological regulation negative regulation of biological process regulation of programmed cell death ketone metabolic process metabolic process cellular process aldehyde metabolic process methylglyoxal metabolic process carbohydrate metabolic process primary metabolic process regulation of biological process regulation of cellular process negative regulation of programmed cell death regulation of apoptotic process biological regulation negative regulation of biological process regulation of programmed cell death cell death negative regulation of apoptotic process negative regulation of cellular process apoptotic process programmed cell death developmental process myeloid leukocyte differentiation cellular developmental process hemopoiesis cell development myeloid cell differentiation cell differentiation osteoclast differentiation anatomical structure development leukocyte differentiation RNA metabolic process regulation of primary metabolic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process transcription by RNA polymerase II regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of transcription by RNA polymerase II regulation of biosynthetic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of gene expression biosynthetic process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process glutathione metabolic process modified amino acid metabolic process sulfur compound metabolic process amide metabolic process	extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cell periphery extracellular exosome membrane-bounded organelle extracellular vesicle cellular anatomical structure extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen nuclear lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR037523	Vicinal oxygen chelate (VOC) domain	Domain
A, B	IPR029068	Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase	Homologous Superfamily
A, B	IPR018146	Glyoxalase I, conserved site	Conserved Site
A, B	IPR004360	Glyoxalase/fosfomycin resistance/dioxygenase domain	Domain
A, B	IPR004361	Glyoxalase I	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: Q04760	esophageal squamous cell carcinoma melanoma melancholia endogenous depression plasma cell myeloma anxiety disorder Anxiety States, Neurotic bipolar disorder depressive disorder neurotic disorder schizophrenia autism cutaneous melanoma lung cancer osteosarcoma esophageal squamous cell carcinoma melanoma melancholia endogenous depression plasma cell myeloma anxiety disorder Anxiety States, Neurotic bipolar disorder depressive disorder neurotic disorder schizophrenia autism cutaneous melanoma lung cancer osteosarcoma malignant colon neoplasm

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A, B	lactoylglutathione lyase M-CSA #32	Lactoyl-glutathione lyase (or glyoxalase I) is part of the glyoxalase system which catalyses the conversion of acyclic alpha-oxoaldehydes into the corresponding alpha-hydroxyacids. Glyoxalase I catalyses the isomerization of the hemithioacetal (formed spontaneously from alpha-oxoaldehyde and GSH), to S-2-hydroxyacylglutathione (or R) derivatives, therefore decreasing the steady-state concentrations of physiological alpha-oxoaldehydes and associated glycation reactions. Physiological substrates of glyoxalase I are methylglyoxal, glyoxal and other acyclic alpha-oxoaldehydes. This is the first of two steps in the conversion of 2-oxo-aldehydes to the corresponding 2-hydroxycarboxylic acids by way of the glyoxylase system. Methylglyoxal is produced as a by product of the triosephosphate isomerase reaction in glycolysis and, if not removed, is toxic as it reacts readily with with proteins and nucleic acids.	Defined by 4 residues: GLN:A-33GLU:A-99HIS:B-126GLU:B-172 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.4.1.5 (PDB Primary Data) Search M-CSA Motif + EC 4.4.1.5

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.